ID A0A452DI36_BOVIN Unreviewed; 752 AA.
AC A0A452DI36;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=5-aminolevulinate synthase, non-specific, mitochondrial {ECO:0000256|ARBA:ARBA00039790};
DE EC=2.3.1.37 {ECO:0000256|ARBA:ARBA00013257};
DE AltName: Full=5-aminolevulinic acid synthase 1 {ECO:0000256|ARBA:ARBA00042303};
DE AltName: Full=Delta-ALA synthase 1 {ECO:0000256|ARBA:ARBA00042219};
DE AltName: Full=Delta-aminolevulinate synthase 1 {ECO:0000256|ARBA:ARBA00042079};
GN Name=ALAS1 {ECO:0000313|Ensembl:ENSBTAP00000005380.6,
GN ECO:0000313|VGNC:VGNC:25803};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000005380.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000005380.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000005380.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000005380.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000005380.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent
CC condensation of succinyl-CoA and glycine to form aminolevulinic acid
CC (ALA), with CoA and CO2 as by-products.
CC {ECO:0000256|ARBA:ARBA00037218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA;
CC Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:356416; EC=2.3.1.37;
CC Evidence={ECO:0000256|ARBA:ARBA00033616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12922;
CC Evidence={ECO:0000256|ARBA:ARBA00033616};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from glycine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005029}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004637}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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DR AlphaFoldDB; A0A452DI36; -.
DR SMR; A0A452DI36; -.
DR Ensembl; ENSBTAT00000005380.6; ENSBTAP00000005380.6; ENSBTAG00000004118.6.
DR VEuPathDB; HostDB:ENSBTAG00000004118; -.
DR VGNC; VGNC:25803; ALAS1.
DR GeneTree; ENSGT00940000156030; -.
DR InParanoid; A0A452DI36; -.
DR OMA; RAYFSGM; -.
DR Reactome; R-BTA-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00375.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000004118; Expressed in cardiac ventricle and 105 other cell types or tissues.
DR ExpressionAtlas; A0A452DI36; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003870; F:5-aminolevulinate synthase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0048821; P:erythrocyte development; IBA:GO_Central.
DR GO; GO:0006784; P:heme A biosynthetic process; IEA:Ensembl.
DR GO; GO:0006785; P:heme B biosynthetic process; IEA:Ensembl.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0048034; P:heme O biosynthetic process; IEA:Ensembl.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1903412; P:response to bile acid; IEA:Ensembl.
DR CDD; cd06454; KBL_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010961; 4pyrrol_synth_NH2levulA_synth.
DR InterPro; IPR015118; 5aminolev_synth_preseq.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01821; 5aminolev_synth; 1.
DR PANTHER; PTHR13693:SF50; 5-AMINOLEVULINATE SYNTHASE, NON-SPECIFIC, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF09029; Preseq_ALAS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 107..250
FT /note="5-aminolevulinate synthase presequence"
FT /evidence="ECO:0000259|Pfam:PF09029"
FT DOMAIN 358..701
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 166..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 82769 MW; 64E6E5F1C87F8F0D CRC64;
MKVSAPVQHC TSSPLLAVPV IQSKSKERLL ASPRPALSAA RLRRSRTRPR RMRSCPSECI
LGRQGSRPEG SCRQGQGLVR RFHLGTCGLR HLRRVPRAGS VYLREMETVV RRCPFLSRVP
QAFLQKAGKS LLFYAQNCPK MMEIGAKPAP RALSTSAVLC QQVTETPPAN EKDKAAKAEV
QQAPDGSQQA PDGSQQTADG TQLPSGHPSL ASSQGTGSKC PFLAAEMSQG GSSVFRKASL
ALQEDVQEMH AVREEVAQTS VNPSVINVKT EGGELNGLLK NFQDIMRKQR PERVSHLLQD
NLPKSVCTFQ YDRFFEKKID EKKNDHSYRV FKTVNRKAQC FPMADDYSDS LISKKQVSVW
CSNDYLGMSR HPRVCGAVID TLKQHGTGAG GTRNISGTSK FHVDLEQELA DLHGKDAALL
FSSCFVANDS TLFTLAKMMP GCEIYSDAGN HASMIQGIRN SGVPKYIFRH NDVSHLRELL
QRSDPAVPKI VAFETVHSMD GAVCPLEELC DVAHEFGAIT FVDEVHAVGL YGLQGGGIGD
RDGVMPKMDI ISGTLGKAIG CVGGYIASTS SLIDTVRSYA AGFIFTTSLP PMLLAGALES
VRILRSTEGR TLRRQHQRNV KLMRQMLMDA GLPVVHCPSH IIPVRVADAA KNTEVCDELM
TRHNIYVQAI NYPTVPRGEE LLRIAPTPHH TPQMMSYFVD NLLATWKRVG LELKPHSSAE
CNFCRRPLHF EMMSEREKSY FSGMSKLVSA QA
//
